This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5ol2
From Proteopedia
(Difference between revisions)
m (Protected "5ol2" [edit=sysop:move=sysop]) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | The | + | ==The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile== |
| + | <StructureSection load='5ol2' size='340' side='right'caption='[[5ol2]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ol2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OL2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ol2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ol2 OCA], [https://pdbe.org/5ol2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ol2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ol2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ol2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A125V455_CLODI A0A125V455_CLODI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The electron transferring flavoprotein/butyryl-CoA dehydrogenase (EtfAB/Bcd) catalyzes the reduction of one crotonyl-CoA and two ferredoxins by two NADH within a flavin-based electron-bifurcating process. Here we report on the X-ray structure of the Clostridium difficile (EtfAB/Bcd)4 complex in the dehydrogenase-conducting D-state, alpha-FAD (bound to domain II of EtfA) and delta-FAD (bound to Bcd) being 8 A apart. Superimposing Acidaminococcus fermentans EtfAB onto C. difficile EtfAB/Bcd reveals a rotation of domain II of nearly 80 degrees . Further rotation by 10 degrees brings EtfAB into the bifurcating B-state, alpha-FAD and beta-FAD (bound to EtfB) being 14 A apart. This dual binding mode of domain II, substantiated by mutational studies, resembles findings in non-bifurcating EtfAB/acyl-CoA dehydrogenase complexes. In our proposed mechanism, NADH reduces beta-FAD, which bifurcates. One electron goes to ferredoxin and one to alpha-FAD, which swings over to reduce delta-FAD to the semiquinone. Repetition affords a second reduced ferredoxin and delta-FADH(-), which reduces crotonyl-CoA. | ||
| - | + | The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile.,Demmer JK, Pal Chowdhury N, Selmer T, Ermler U, Buckel W Nat Commun. 2017 Nov 17;8(1):1577. doi: 10.1038/s41467-017-01746-3. PMID:29146947<ref>PMID:29146947</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ol2" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridioides difficile]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Buckel W]] | ||
| + | [[Category: Chowdhury NP]] | ||
| + | [[Category: Demmer JK]] | ||
| + | [[Category: Ermler U]] | ||
| + | [[Category: Selmer T]] | ||
Current revision
The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile
| |||||||||||
